Failure of rabbit reticulocytes to incorporate conalbumin or lactoferrin iron

• Published in: Biochimica et biophysica acta Vol. 421; no. 1; pp. 80 - 86
• Main Authors: Zapolski, E.J., Princiotto, J.V.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 14.01.1976
• Subjects: animal science; Animals; Binding Sites; Conalbumin - metabolism; Egg Proteins - metabolism; Humans; Iron - metabolism; Kinetics; Lactoferrin - metabolism; Lactoglobulins - metabolism; livestock; Protein Binding; Rabbits; Reticulocytes - metabolism; Species Specificity; Transferrin - metabolism; zoology
• ISSN: 0304-4165; 0006-3002; 1872-8006; 1878-2434
• DOI: 10.1016/0304-4165(76)90171-9

Despite the remarkable molecular similarity of human lactoferrin and human transferrin, the results of this investigation indicate that human lactoferrin was unable to furnish rabbit reticulocytes with iron for heme synthesis. Although conalbumin closely resembles transferrin in many of its properties, conalbumin iron-binding differs from human transferrin iron-binding. There are conflicting reports in the literature regarding conalbumin's ability to furnish iron to reticulocytes. In this study, small amounts of lactoferrin or conalbumin were adsorbed to mature and immature cell surfaces but neither of these iron-binding proteins surrendered iron intracellularly to reticulocytes for heme synthesis.